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6TBW

Crystal structure of AmpC from E.coli with Avibactam

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PGE A 401
ChainResidue
ATRP93
ALEU131
AHOH723

site_idAC2
Number of Residues15
Detailsbinding site for residue NXL A 402
ChainResidue
ATHR316
AGLY317
AALA318
AASN346
AHOH501
AHOH641
AHOH669
AHOH728
AHOH749
ASER64
AGLN120
ATYR150
AASN152
ALEU293
ALYS315

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS13
AHIS13
AHIS13
ACL405
ACL405
ACL405

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 404
ChainResidue
AHIS186
AHOH523
AHOH525
AHOH716
AHOH768

site_idAC5
Number of Residues9
Detailsbinding site for residue CL A 405
ChainResidue
AHIS13
AHIS13
AHIS13
AZN403
AZN403
AZN403
AHOH853
AHOH853
AHOH853

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201
ChainResidueDetails
ASER64

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
ATYR150
AASN152
AALA318

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PDB entries from 2024-07-17

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